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Improving the stability of chondroitinase ABC I via interaction with gold nanorods.

Authors :
Naderi MS
Moghadam TT
Khajeh K
Ranjbar B
Source :
International journal of biological macromolecules [Int J Biol Macromol] 2018 Feb; Vol. 107 (Pt A), pp. 297-304. Date of Electronic Publication: 2017 Sep 01.
Publication Year :
2018

Abstract

Chondroitinase ABC I (cABC I) cleaves glycosaminoglycan chains which are responsible for most of the inhibition of axon regrowth in spinal cord injury. The application of chondroitinase ABC I (cABC I) in damaged nervous tissue is found to prune glycosaminoglycan chains of proteoglycans and facilitate axon regeneration. However, a limiting factor for such application is the enzyme's instability. In this study, the structure and activity of cABC I have been investigated upon interaction with various concentrations of Gold nanorods. The enzyme preserved its major activity with increase in substrate affinity in the presence of the nanostructures. Analysis of circular dichroism spectropolarimetry data showed that secondary structural content of the enzyme slightly increased. The complex form of the enzyme also showed higher storage stability. Fluorescence studies indicated that enzyme obtained more rigidity in its structure. Taking higher stability of enzyme upon interaction, result of this investigation interaction paves the way for utilizing tiny plasmonic nanostructures for fruitful applications in biomedicine.<br /> (Copyright © 2017. Published by Elsevier B.V.)

Details

Language :
English
ISSN :
1879-0003
Volume :
107
Issue :
Pt A
Database :
MEDLINE
Journal :
International journal of biological macromolecules
Publication Type :
Academic Journal
Accession number :
28867227
Full Text :
https://doi.org/10.1016/j.ijbiomac.2017.08.167